Structural and drug-binding properties of α1-acid glycoprotein in reverse micelles

Nishi, Koji; Sakai, Norifumi; Komine, Yoshio; Maruyama, Toru; Halsall, H. Brian; Otagiri, Masaki

doi:10.1016/s1570-9639(02)00465-x

Cited by 34 publications

(51 citation statements)

References 33 publications

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“…Lipocalins linked to membranes through other mechanisms have been reported in bacteria and plants (Bishop et al, 2006;Charron and Sarhan, 2006), and indirect interactions of Lipocalins with membranes have been described for a1-acid-glicoprotein (Nishi et al, 2002), b-Lactoglobulin (Martins et al, 2008) and Tear Lipocalin (Saaren-Seppala et al, 2005). These data point to the existence of membrane receptors for Lipocalins, some of which have been already characterized, mostly for vertebrate Lipocalins (Hvidberg et al, 2005;Kawaguchi et al, 2007;Wojnar et al, 2001), but also for Insecticyanin in M. sexta (Kang et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Grasshopper Lazarillo, a GPI-anchored Lipocalin, increases Drosophila longevity and stress resistance, and functionally replaces its secreted homolog NLaz

Ruiz

Wicker-Thomas

Sánchez

et al. 2012

Insect Biochemistry and Molecular Biology

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Section: Introductionmentioning

confidence: 99%

Grasshopper Lazarillo, a GPI-anchored Lipocalin, increases Drosophila longevity and stress resistance, and functionally replaces its secreted homolog NLaz

Ruiz

Wicker-Thomas

Sánchez

et al. 2012

Insect Biochemistry and Molecular Biology

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“…It is known that hAGP has the binding sites for acidic and basic ligands and steroid hormones, respectively, and these sites overlap each other (Maruyama et al, 1990). To investigate the binding capacity of rhAGP to three drugs, chlorpromazine, warfarin, and progesterone, the values of n, the number of binding site, and K a , association constant, were calculated using the tryptophan fluorescence quenching method (Nishi et al, 2002). Figure 6 shows the titration curves of tryptophanyl fluorescence intensity using chlorpromazine as a typical example.…”

Section: Resultsmentioning

confidence: 99%

“…Drug-binding parameters were calculated using the dmd.aspetjournals.org tryptophan fluorescence quenching method (Nishi et al, 2002). We obtained a fluorometric titration curve by plotting the tryptophanyl fluorescence intensity of AGP (excitation ϭ 295 nm) using a Jasco FP-770 fluorometer.…”

Section: Expression Of Rhagpmentioning

confidence: 99%

CONSTRUCTION OF EXPRESSION SYSTEM FOR HUMAN α₁-ACID GLYCOPROTEIN INPICHIA PASTORISAND EVALUATION OF ITS DRUG-BINDING PROPERTIES

Nishi¹,

Fukunaga²,

Otagiri³

2004

Drug Metab Dispos

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ABSTRACT:Human ␣ 1 -acid glycoprotein (hAGP) is a plasma glycoprotein that functions as a major carrier of basic ligands. This is the first report of the recombinant hAGP (rhAGP). In this study, rhAGP was expressed in the methylotropic yeast Pichia pastoris (GS115) using the expression vector, pPIC9, and then purified by anionic exchange, hydrophobic interaction, and gel filtration chromatography. The molecular weight of rhAGP was much lower than that of hAGP, because of the difference in glycan chain content. Results of glycopeptidase F digestion suggest that the peptide moiety of rhAGP was the same as that of hAGP. The results of circular dichroism spectra measurement indicated that rhAGP predominantly formed a ␤-sheet-rich structure that was the same as that of hAGP and typical of the lipocalin family. From the experiments using AGP-binding drugs (chlorpromazine, warfarin, and progesterone) and quinaldine red as a probe for the binding site, it was indicated that rhAGP also had the same ligand-binding capacity and binding site structure as hAGP. These findings strongly suggest that this recombinant hAGP (rhAGP) is very useful for the exploration of the ligand-binding site and biological function of hAGP.

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“…70 The drug-binding capacity of AGP is known to decrease due to its interaction with biomembranes accompanying its conformational changes. 71,72 AGP is a difficult target in X-ray crystallography and NMR spectroscopy because it is a polypeptide consisting of 183 amino acids with 5 glycan chains that constitute about 40% of the total mass (36 kDa). Therefore, to elucidate the membrane-induced conformational change of AGP, we measured the VUVCD spectra of AGP and constituent sugars in the presence or absence of liposome (L-¡-phosphatidyl-DL-glycerol).…”

Section: Membrane-induced Conformational Change Of Agpmentioning

confidence: 99%

Construction of a Synchrotron-Radiation Vacuum-Ultraviolet Circular-Dichroism Spectrophotometer and Its Application to the Structural Analysis of Biomolecules

Matsuo

Gekko

2013

Bulletin of the Chemical Society of Japan

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A vacuum-ultraviolet (VUV) circular-dichroism (CD) spectrophotometer usable down to 140 nm was constructed using synchrotron radiation and applied to the structural analyses of various saccharides, amino acids, and proteins in aqueous solutions. Most monosaccharides and disaccharides exhibited a positive CD peak around 170 nm, depending on anomeric and axial/equatorial configurations of hydroxy groups, transgauche configurations of hydroxymethyl groups, and the type of glycosidic linkage. The VUVCD spectra of glycosaminoglycans sensitively reflected the characteristic contributions of constituent functional groups in the VUV region. L-Isomers of amino acids showed two successive positive peaks around 200 and 180 nm, depending on the types of side chains. The VUVCD spectrum of alanine theoretically calculated using a time-dependent density functional theory revealed the important role of hydration for stabilizing the alanine structure. The VUVCD spectra of native proteins down to 160 nm improved the predictive accuracy for the contents, numbers of segments, and sequences of ¡-helices and ¢-strands. These secondary-structure analyses were also successfully applied to various types of nonnative proteins. The obtained results demonstrate that synchrotronradiation VUVCD spectroscopy is a powerful technique for the structural analysis of biomolecules in aqueous solution, and hence could open a new field in structural biology.

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Structural and drug-binding properties of α1-acid glycoprotein in reverse micelles

Cited by 34 publications

References 33 publications

Grasshopper Lazarillo, a GPI-anchored Lipocalin, increases Drosophila longevity and stress resistance, and functionally replaces its secreted homolog NLaz

Grasshopper Lazarillo, a GPI-anchored Lipocalin, increases Drosophila longevity and stress resistance, and functionally replaces its secreted homolog NLaz

CONSTRUCTION OF EXPRESSION SYSTEM FOR HUMAN α₁-ACID GLYCOPROTEIN INPICHIA PASTORISAND EVALUATION OF ITS DRUG-BINDING PROPERTIES

Construction of a Synchrotron-Radiation Vacuum-Ultraviolet Circular-Dichroism Spectrophotometer and Its Application to the Structural Analysis of Biomolecules

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Structural and drug-binding properties of α1-acid glycoprotein in reverse micelles

Cited by 34 publications

References 33 publications

Grasshopper Lazarillo, a GPI-anchored Lipocalin, increases Drosophila longevity and stress resistance, and functionally replaces its secreted homolog NLaz

Grasshopper Lazarillo, a GPI-anchored Lipocalin, increases Drosophila longevity and stress resistance, and functionally replaces its secreted homolog NLaz

CONSTRUCTION OF EXPRESSION SYSTEM FOR HUMAN α1-ACID GLYCOPROTEIN INPICHIA PASTORISAND EVALUATION OF ITS DRUG-BINDING PROPERTIES

Construction of a Synchrotron-Radiation Vacuum-Ultraviolet Circular-Dichroism Spectrophotometer and Its Application to the Structural Analysis of Biomolecules

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Product

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About

CONSTRUCTION OF EXPRESSION SYSTEM FOR HUMAN α₁-ACID GLYCOPROTEIN INPICHIA PASTORISAND EVALUATION OF ITS DRUG-BINDING PROPERTIES